Journal
PRION
Volume 3, Issue 4, Pages 202-205Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/pri.3.4.10012
Keywords
prion protein; PrPC; extracellular matrix; cell adhesion molecules; neuritogenesis; p59fyn; Ca2+
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Funding
- Italian Ministero dell'Universita e della Ricerca [Prin 2006]
- University of Padova [CPDA089551]
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Tens of putative interacting partners of the cellular prion protein (PrPC) have been identified, yet the physiologic role of PrPC remains unclear. For the first time, however, a recent paper has demonstrated that the absence of PrPC produces a lethal phenotype. Starting from this evidence, here we discuss the validity of past and more recent literature supporting that, as part of protein platforms at the cell surface, PrPC may bridge extracellular matrix molecules and/or membrane proteins to intracellular signaling pathways.
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